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Histone H2A.X (Ser139) Blocking Peptide

Synthetic peptide

     
  • SPECIFICATION
  • CITATIONS
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Product Information
Primary Accession P16104
Additional Information
Gene ID 3014
Other Names Histone H2AX, H2a/x, Histone H2AX, H2AFX, H2AX
Target/Specificity The synthetic peptide sequence is selected from aa 134-143 of HUMAN H2AFX
Format Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name H2AFX
Synonyms H2AX
Function Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C- terminal phosphorylation.
Cellular Location Nucleus Chromosome
Research Areas
Citations (0)

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Background

Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C- terminal phosphorylation.

References

Mannironi C.,et al.Nucleic Acids Res. 17:9113-9126(1989).
Ebert L.,et al.Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
Rogakou E.P.,et al.J. Biol. Chem. 273:5858-5868(1998).
Rogakou E.P.,et al.J. Cell Biol. 146:905-916(1999).
Paull T.T.,et al.Curr. Biol. 10:886-895(2000).

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$ 80.00
Cat# BP20703b
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